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Chlamydia pneumoniae effector chlamydial outer protein N sequesters fructose bisphosphate aldolase A, providing a benefit to bacterial growth

Overview of attention for article published in BMC Microbiology, December 2014
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Title
Chlamydia pneumoniae effector chlamydial outer protein N sequesters fructose bisphosphate aldolase A, providing a benefit to bacterial growth
Published in
BMC Microbiology, December 2014
DOI 10.1186/s12866-014-0330-3
Pubmed ID
Authors

Kasumi Ishida, Junji Matsuo, Yoshimasa Yamamoto, Hiroyuki Yamaguchi

Abstract

BackgroundPathogenic chlamydiae are obligate intracellular pathogens and have adapted successfully to human cells, causing sexually transmitted diseases or pneumonia. Chlamydial outer protein N (CopN) is likely a critical effector protein secreted by the type III secretion system in chlamydiae, which manipulates host cells. However, the mechanisms of its action remain to be clarified. In this work, we aimed to identify previously unidentified CopN effector target in host cells.ResultsWe first performed a pull-down assay with recombinant glutathione S-transferase (GST) fusion CopN proteins (GST¿CpCopN: Chlamydia pneumoniae TW183, GST¿CtCopN: Chlamydia trachomatis D/UW-3/CX) as ¿bait¿ and soluble lysates obtained from human immortal epithelial HEp-2 cells as ¿prey¿, followed by SDS-PAGE with mass spectroscopy (MS). We found that a host cell protein specifically bound to GST¿CpCopN, but not GST¿CtCopN. MS revealed the host protein to be fructose bisphosphate aldolase A (aldolase A), which plays a key role in glycolytic metabolism. We also confirmed the role of aldolase A in chlamydia-infected HEp-2 cells by using two distinct experiments for gene knockdown with an siRNA specific to aldolase A transcripts, and for assessment of glycolytic enzyme gene expression levels. As a result, both the numbers of chlamydial inclusion-forming units and RpoD transcripts were increased in the chlamydia-infected aldolase A knockdown cells, as compared with the wild-type HEp-2 cells. Meanwhile, chlamydial infection tended to enhance expression of aldolase A.ConclusionsWe discovered that one of the C. pneumoniae CopN targets is the glycolytic enzyme aldolase A. Sequestering aldolase A may be beneficial to bacterial growth in infected host cells.

Twitter Demographics

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Mendeley readers

The data shown below were compiled from readership statistics for 6 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 6 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 2 33%
Other 1 17%
Student > Bachelor 1 17%
Student > Postgraduate 1 17%
Student > Ph. D. Student 1 17%
Other 0 0%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 33%
Computer Science 1 17%
Nursing and Health Professions 1 17%
Unspecified 1 17%
Medicine and Dentistry 1 17%
Other 0 0%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 22 December 2014.
All research outputs
#3,034,996
of 4,691,823 outputs
Outputs from BMC Microbiology
#614
of 925 outputs
Outputs of similar age
#97,450
of 155,138 outputs
Outputs of similar age from BMC Microbiology
#34
of 49 outputs
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So far Altmetric has tracked 925 research outputs from this source. They receive a mean Attention Score of 2.7. This one is in the 28th percentile – i.e., 28% of its peers scored the same or lower than it.
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We're also able to compare this research output to 49 others from the same source and published within six weeks on either side of this one. This one is in the 24th percentile – i.e., 24% of its contemporaries scored the same or lower than it.